ID A0A087YJ93_POEFO Unreviewed; 829 AA.
AC A0A087YJ93;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000632};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000632};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000018096.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000018096.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001149,
CC ECO:0000256|PIRNR:PIRNR000632};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|PIRNR:PIRNR000632}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000256|PIRNR:PIRNR000632}.
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DR EMBL; AYCK01003724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01003725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01003726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01003727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087YJ93; -.
DR Ensembl; ENSPFOT00000018118.1; ENSPFOP00000018096.1; ENSPFOG00000017969.2.
DR GeneTree; ENSGT00940000158881; -.
DR OMA; QNTENMY; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07685; F-BAR_Fes; 1.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF197; TYROSINE-PROTEIN KINASE FES_FPS; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF000632; TyrPK_fps; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000632, ECO:0000256|PIRSR:PIRSR000632-
KW 2};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|PIRNR:PIRNR000632};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR000632};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000632};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000632,
KW ECO:0000256|PIRSR:PIRSR000632-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000632};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000632}.
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 466..555
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 567..828
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 139..173
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 690
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-1"
FT BINDING 573..581
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 829 AA; 95554 MW; 4FF3B169854CBF0B CRC64;
MGFGEDLRCP QAHAAVMRLL DSELHLMEIM KKWMGQRAKS EREFSVQLHQ MTAMAEKMDR
PQTNPGADYI SQLNKSWGVL VSQTESLSQV MRRRSEELLD GPISKLTLLI RDKQQLRKTY
AEHWNLLRQE LNKVTHTELE RLKTSYRQAV KDAALARRKY QDMSKDKERE KNRERYIKAS
LKLHELHNEY VLSVQAAQVY HQHHYSQMQP ALLSALQTLQ QEMVLILKEI LQEYFDISTL
LQQEVVKVHR EMSSALIAID PHREYESFTQ QNRSVGEIPV CVDFDCSLLE DTEQLKPKEI
ELNDLTLETI QHKLTAIEEE LLALARSLGS QQTSVEQLEL ELENEVDGNK KGQRVYQFSK
RHAMEECRQQ VALSQGIKAK LEVQRLLLKE KLDQLGFREP PQALRLDMDS VSLLSSTSND
NVQTSGKILV DGIINNLSNL FRHKSETPAS TSKDPEVDRP LSQQDWYHGA IPRLEVQQLL
QNDGDFLVRK SQEKQVYVIS VQWEGSCKHF LIQYMDNLYR LDGEGFHSIP KLINHLQMSR
LPVTKKSEAI LKKPILKDKW VLEHDDIVLG PLIGKGNFGE VYSGRLRSDN TPVAVKSCKE
NLAPEHKSKF LMEARSILKQ YNHPNIVKLI GVCTQKQPIY IIMELVSGGD FLSFLRTEGH
SLTPKMLVKM TENVAAGMEY LEIKKCIHRD LAARNCLVAE RNVVKISDFG MSRERDDGVY
SAEGGLRQIP VKWTAPEALN YGRYTTQSDV WSFGILLWET FSMGMTPYTS MNNQQTRDEV
EKGYRMPAPH GCPMEISRVM NNCWQYDPKN RPTFRKIRAE LNAIHNKIT
//
